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Arginine and ornithine oxidation catalyzed by lentil seedling copper-amine oxidase
R Medda1, A Padiglia, A Lorrai
1Department of Sciences Applied to Biosystems, University of Cagliari, Italy.
Journal of Protein Chemistry
|July 6, 2000
Abstract:
The oxidation of L-ornithine and L-arginine catalyzed by lentil (Lens esculenta) seedling copper-amine oxidase has been investigated by polarographic techniques, optical spectroscopy, and capillary electrophoresis. Both L-ornithine and L-arginine were found to be poor substrates for lentil amine oxidase. L-Ornithine was oxidized to glutamate-5-semialdehyde and ammonia, in similar manner as usual substrates. Glutamate-5-semialdehyde spontaneously cyclizes to delta1-pyrroline-5-carboxylic acid. Arginine is oxidized by an unusual mechanism yielding glutamate-5-semialdehyde, ammonia, and urea as reaction products.